Elsevier

Neuroscience Letters

Volume 313, Issue 3, 9 November 2001, Pages 129-132
Neuroscience Letters

Group I metabotropic glutamate receptors control phosphorylation of CREB, Elk-1 and ERK via a CaMKII-dependent pathway in rat striatum

https://doi.org/10.1016/S0304-3940(01)02258-3Get rights and content

Abstract

In vivo activation of group I metabotropic glutamate receptors (mGluRs) upregulates phosphorylation of cyclic AMP response element-binding protein (CREB), Elk-1 and extracellular signal-regulated kinases (ERK) in striatal neurons. To evaluate putative roles of Ca2+/calmodulin-dependent protein kinase II (CaMKII) in CREB, Elk-1 and ERK phosphorylation, the CaMKII inhibitor, KN62, was infused simultaneously with the group I mGluR agonist, 3,5-dihydroxyphenylglycine (DHPG), into the rat dorsal striatum. The results showed that DHPG (125, 250, and 500 nmol) increased phosphorylated (p) CaMKII immunoreactivity (IR) in a dose-dependent manner. KN62 (50 nmol) significantly attenuated 500 nmol DHPG-induced pERK, pElk-1 and pCREB IR in the ipsilateral dorsal striatum. These data indicate that pCaMKII is a possible upstream effector that is responsible for the regulation of CREB, Elk-1 and ERK phosphoproteins in response to group I mGluR stimulation in striatal neurons.

Section snippets

Acknowledgements

This work was supported by grants from the NIH (DA10355 and MH61469) and University of Missouri-Research Board.

References (17)

There are more references available in the full text version of this article.

Cited by (58)

  • A3 adenosine receptor agonist IB-MECA reverses chronic cerebral ischemia-induced inhibitory avoidance memory deficit

    2022, European Journal of Pharmacology
    Citation Excerpt :

    A3 adenosine receptor activation was previously reported to inhibit metabotropic glutamate receptor function (Macek et al., 1998). Furthermore, the metabotropic glutamate receptor can functionally regulate ERK activation (Choe and Wang, 2001; Ferraguti et al., 1999; Karim et al., 2001), resulting in phosphorylation of MAP-2 and altered microtubule binding/stabilization (Sanchez et al., 2000). Previous studies have reported neuroprotective actions of IB-MECA following cerebral ischemia.

  • FMRP and the Pathophysiology of Fragile X Syndrome

    2016, Neuronal and Synaptic Dysfunction in Autism Spectrum Disorder and Intellectual Disability
  • Metabotropic glutamate receptor 5 upregulates surface NMDA receptor expression in striatal neurons via CaMKII

    2015, Brain Research
    Citation Excerpt :

    These data demonstrate a subtype specific role of mGluR5 in regulating surface and intracellular GluN1/GluN2B receptor expression in striatal neurons. DHPG or mGluR5 positive allosteric modulators readily activated CaMKIIα in rat hippocampal, cortical and striatal neurons (Choe and Wang, 2001; Mockett et al., 2011; Uslaner et al., 2009; Jin et al., 2013b). Moreover, mGluR5 but not mGluR1 activity-dependently recruited active CaMKIIα to adjacent GluN2B subunits, enabling CaMKIIα to phosphorylate GluN2B at a CaMKIIα-sensitive site (S1303), based on a stepwise model recently established in striatal neurons (Jin et al., 2013b).

  • The therapeutic potential of G-protein coupled receptors in Huntington's disease

    2010, Pharmacology and Therapeutics
    Citation Excerpt :

    ERK may be activated via several pathways, including transactivation of receptor tyrosine kinases, βγ-mediated activation of the phosphatidyl inositol 3-kinase pathway, or via cAMP-dependent mechanisms (Reviewed in Roux & Blenis, 2004). The latter two pathways link GPCRs to the regulation of ERK activity, and GPCRs known to couple to ERK include A2A, CB1, D1, D2, GABAB, and mGluR (Balasubramanian et al., 2004; Bouaboula et al., 1995; Brami-Cherrier et al., 2002; Choe & Wang, 2001; Luo et al., 1998; Schulte & Fredholm, 2000). In cell models of HD, a protective role for ERK activation has been demonstrated in several studies.

View all citing articles on Scopus
View full text